TY - JOUR A1 - Sloan, Katherine E. A1 - Leisegang, Matthias A1 - Döbele, Carmen A1 - Ramírez, Ana S. A1 - Simm, Stefan A1 - Safferthal, Charlotta A1 - Kretschmer, Jens A1 - Schorge, Tobias A1 - Markoutsa, Stavroula A1 - Haag, Sara A1 - Karas, Michael A1 - Ebersberger, Ingo A1 - Schleiff, Enrico A1 - Watkins, Nicholas J. A1 - Bohnsack, Markus T. T1 - The association of late-acting snoRNPs with human pre-ribosomal complexes requires the RNA helicase DDX21 T2 - Nucleic Acids Research N2 - Translation fidelity and efficiency require multiple ribosomal (r)RNA modifications that are mostly mediated by small nucleolar (sno)RNPs during ribosome production. Overlapping basepairing of snoRNAs with pre-rRNAs often necessitates sequential and efficient association and dissociation of the snoRNPs, however, how such hierarchy is established has remained unknown so far. Here, we identify several late-acting snoRNAs that bind pre-40S particles in human cells and show that their association and function in pre-40S complexes is regulated by the RNA helicase DDX21. We map DDX21 crosslinking sites on pre-rRNAs and show their overlap with the basepairing sites of the affected snoRNAs. While DDX21 activity is required for recruitment of the late-acting snoRNAs SNORD56 and SNORD68, earlier snoRNAs are not affected by DDX21 depletion. Together, these observations provide an understanding of the timing and ordered hierarchy of snoRNP action in pre-40S maturation and reveal a novel mode of regulation of snoRNP function by an RNA helicase in human cells. Y1 - 2014 UR - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/37219 UR - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-372194 SN - 1362-4962 SN - 0305-1048 N1 - © The Author(s) 2014. Published by Oxford University Press on behalf of Nucleic Acids Research. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com VL - 43 IS - 1 SP - 553 EP - 564 PB - Oxford Univ. Press CY - Oxford ER -